Function of glutathione peroxidases in legume root nodules

[EN] Glutathione peroxidases (Gpxs) are antioxidant enzymes not studied so far in legume nodules, despite the fact that reactive oxygen species are produced at different steps of the symbiosis. The function of two Gpxs that are highly expressed in nodules of the model legume Lotus japonicus was exam...

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Autores: Matamoros, Manuel A., SAIZ ANDRES, ANA, Peñuelas, Maria, Bustos-Sanmamed, Pilar, Barja, Maria V., Rouhier, Nicolas, Moore, Marten, James, Euan K., Dietz, Karl-Josef, Becana, Manuel, Mulet, José Miguel|||0000-0002-9087-3838
Tipo de recurso: artículo
Fecha de publicación:2015
País:España
Institución:Universitat Politècnica de València (UPV)
Repositorio:RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
Idioma:inglés
OAI Identifier:oai:riunet.upv.es:10251/67899
Acceso en línea:https://riunet.upv.es/handle/10251/67899
Access Level:acceso abierto
Palabra clave:Antioxidants
Glutathione peroxidases
Legume nodules
Lotus japonicus
Nitric oxide
Reactive oxygen species
S-nitrosylation
BIOQUIMICA Y BIOLOGIA MOLECULAR
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network_acronym_str ES
network_name_str España
repository_id_str
dc.title.none.fl_str_mv Function of glutathione peroxidases in legume root nodules
title Function of glutathione peroxidases in legume root nodules
spellingShingle Function of glutathione peroxidases in legume root nodules
Matamoros, Manuel A.
Antioxidants
Glutathione peroxidases
Legume nodules
Lotus japonicus
Nitric oxide
Reactive oxygen species
S-nitrosylation
BIOQUIMICA Y BIOLOGIA MOLECULAR
title_short Function of glutathione peroxidases in legume root nodules
title_full Function of glutathione peroxidases in legume root nodules
title_fullStr Function of glutathione peroxidases in legume root nodules
title_full_unstemmed Function of glutathione peroxidases in legume root nodules
title_sort Function of glutathione peroxidases in legume root nodules
dc.creator.none.fl_str_mv Matamoros, Manuel A.
SAIZ ANDRES, ANA
Peñuelas, Maria
Bustos-Sanmamed, Pilar
Barja, Maria V.
Rouhier, Nicolas
Moore, Marten
James, Euan K.
Dietz, Karl-Josef
Becana, Manuel
Mulet, José Miguel|||0000-0002-9087-3838
author Matamoros, Manuel A.
author_facet Matamoros, Manuel A.
SAIZ ANDRES, ANA
Peñuelas, Maria
Bustos-Sanmamed, Pilar
Barja, Maria V.
Rouhier, Nicolas
Moore, Marten
James, Euan K.
Dietz, Karl-Josef
Becana, Manuel
Mulet, José Miguel|||0000-0002-9087-3838
author_role author
author2 SAIZ ANDRES, ANA
Peñuelas, Maria
Bustos-Sanmamed, Pilar
Barja, Maria V.
Rouhier, Nicolas
Moore, Marten
James, Euan K.
Dietz, Karl-Josef
Becana, Manuel
Mulet, José Miguel|||0000-0002-9087-3838
author2_role author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Instituto Universitario Mixto de Biología Molecular y Celular de Plantas
Departamento de Biotecnología
Escuela Técnica Superior de Ingeniería Agronómica y del Medio Natural
Ministerio de Ciencia e Innovación
European Commission
Agence Nationale de la Recherche, Francia
Ministerio de Economía y Competitividad
Repositorio Institucional de la Universitat Politècnica de València Riunet
dc.subject.none.fl_str_mv Antioxidants
Glutathione peroxidases
Legume nodules
Lotus japonicus
Nitric oxide
Reactive oxygen species
S-nitrosylation
BIOQUIMICA Y BIOLOGIA MOLECULAR
topic Antioxidants
Glutathione peroxidases
Legume nodules
Lotus japonicus
Nitric oxide
Reactive oxygen species
S-nitrosylation
BIOQUIMICA Y BIOLOGIA MOLECULAR
description [EN] Glutathione peroxidases (Gpxs) are antioxidant enzymes not studied so far in legume nodules, despite the fact that reactive oxygen species are produced at different steps of the symbiosis. The function of two Gpxs that are highly expressed in nodules of the model legume Lotus japonicus was examined. Gene expression analysis, enzymatic and nitrosylation assays, yeast cell complementation, in situ mRNA hybridization, immunoelectron microscopy, and LjGpx-green fluorescent protein (GFP) fusions were used to characterize the enzymes and to localize each transcript and isoform in nodules. The LjGpx1 and LjGpx3 genes encode thioredoxin-dependent phospholipid hydroperoxidases and are differentially regulated in response to nitric oxide (NO) and hormones. LjGpx1 and LjGpx3 are nitrosylated in vitro or in plants treated with S-nitrosoglutathione (GSNO). Consistent with the modification of the peroxidatic cysteine of LjGpx3, in vitro assays demonstrated that this modification results in enzyme inhibition. The enzymes are highly expressed in the infected zone, but the LjGpx3 mRNA is also detected in the cortex and vascular bundles. LjGpx1 is localized to the plastids and nuclei, and LjGpx3 to the cytosol and endoplasmic reticulum. Based on yeast complementation experiments, both enzymes protect against oxidative stress, salt stress, and membrane damage. It is concluded that both LjGpxs perform major antioxidative functions in nodules, preventing lipid peroxidation and other oxidative processes at different subcellular sites of vascular and infected cells. The enzymes are probably involved in hormone and NO signalling, and may be regulated through nitrosylation of the peroxidatic cysteine essential for catalytic function.
publishDate 2015
dc.date.none.fl_str_mv 2015
2015-05-01
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://riunet.upv.es/handle/10251/67899
url https://riunet.upv.es/handle/10251/67899
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv Ministerio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 PT13%2F0001%2F0008 PLATAFORMA DE RECURSOS BIOMOLECULARES Y BIOINFORMATICOS, PRB2
Ministerio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 AGL2011-24524 SEÑALIZACION POR ESPECIES REACTIVAS DE OXIGENO%2FNITROGENO Y ANTIOXIDANTES EN LA SIMBIOSIS FIJADORA DE NITROGENO RHIZOBIUM-LEGUMINOSA
Agence Nationale de la Recherche, Francia https://doi.org/10.13039/501100001665 ANR-11-LABX-0002 Recherches Avancées sur l'Arbre et les Ecosytèmes Forestiers
Ministerio de Economía y Competitividad http://dx.doi.org/10.13039/501100003329 AGL2014-53717-R FIJACION DE NITROGENO POR LA SIMBIOSIS RIZOBIO-LEGUMINOSA: HEMOGLOBINAS Y MODIFICACIONES OXIDATIVAS DE LAS PROTEINAS DURANTE EL DESARROLLO Y SENESCENCIA DE LOS NODULOS
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Reserva de todos los derechos
http://rightsstatements.org/vocab/InC/1.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Reserva de todos los derechos
http://rightsstatements.org/vocab/InC/1.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Oxford University Press (OUP)
publisher.none.fl_str_mv Oxford University Press (OUP)
dc.source.none.fl_str_mv reponame:RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
instname:Universitat Politècnica de València (UPV)
instname_str Universitat Politècnica de València (UPV)
reponame_str RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
collection RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
repository.name.fl_str_mv
repository.mail.fl_str_mv
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spelling Function of glutathione peroxidases in legume root nodulesMatamoros, Manuel A.SAIZ ANDRES, ANAPeñuelas, MariaBustos-Sanmamed, PilarBarja, Maria V.Rouhier, NicolasMoore, MartenJames, Euan K.Dietz, Karl-JosefBecana, ManuelMulet, José Miguel|||0000-0002-9087-3838AntioxidantsGlutathione peroxidasesLegume nodulesLotus japonicusNitric oxideReactive oxygen speciesS-nitrosylationBIOQUIMICA Y BIOLOGIA MOLECULAR[EN] Glutathione peroxidases (Gpxs) are antioxidant enzymes not studied so far in legume nodules, despite the fact that reactive oxygen species are produced at different steps of the symbiosis. The function of two Gpxs that are highly expressed in nodules of the model legume Lotus japonicus was examined. Gene expression analysis, enzymatic and nitrosylation assays, yeast cell complementation, in situ mRNA hybridization, immunoelectron microscopy, and LjGpx-green fluorescent protein (GFP) fusions were used to characterize the enzymes and to localize each transcript and isoform in nodules. The LjGpx1 and LjGpx3 genes encode thioredoxin-dependent phospholipid hydroperoxidases and are differentially regulated in response to nitric oxide (NO) and hormones. LjGpx1 and LjGpx3 are nitrosylated in vitro or in plants treated with S-nitrosoglutathione (GSNO). Consistent with the modification of the peroxidatic cysteine of LjGpx3, in vitro assays demonstrated that this modification results in enzyme inhibition. The enzymes are highly expressed in the infected zone, but the LjGpx3 mRNA is also detected in the cortex and vascular bundles. LjGpx1 is localized to the plastids and nuclei, and LjGpx3 to the cytosol and endoplasmic reticulum. Based on yeast complementation experiments, both enzymes protect against oxidative stress, salt stress, and membrane damage. It is concluded that both LjGpxs perform major antioxidative functions in nodules, preventing lipid peroxidation and other oxidative processes at different subcellular sites of vascular and infected cells. The enzymes are probably involved in hormone and NO signalling, and may be regulated through nitrosylation of the peroxidatic cysteine essential for catalytic function.AS and PBS were the recipients of predoctoral (Formacion de Personal Investigador) and postdoctoral (Marie Curie) contracts, respectively. We thank Martin Crespi for help with in situ RNA hybridization and Simon Avery for sharing the yeast mutant and for helpful advice. This work was supported by Ministerio de Economia y Competitividad-Fondo Europeo de Desarrollo Regional (AGL2011-24524 and AGL2014-53717-R). The UMR1136 is supported by a grant overseen by the French National Research Agency (ANR) as part of the 'Investissements d'Avenir' programme (ANR-11-LABX-0002-01, Lab of Excellence ARBRE). MM and KJD acknowledge support within SPP1710. The proteomic analysis was performed in the CSIC/UAB Proteomics Facility of IIBB-CSIC that belongs to ProteoRed, PRB2-ISCIII, supported by grant PT13/0001.Oxford University Press (OUP)Instituto Universitario Mixto de Biología Molecular y Celular de PlantasDepartamento de BiotecnologíaEscuela Técnica Superior de Ingeniería Agronómica y del Medio NaturalMinisterio de Ciencia e InnovaciónEuropean CommissionAgence Nationale de la Recherche, FranciaMinisterio de Economía y CompetitividadRepositorio Institucional de la Universitat Politècnica de València Riunet20152015-05-01journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://riunet.upv.es/handle/10251/67899reponame:RiuNet. Repositorio Institucional de la Universitat Politécnica de Valénciainstname:Universitat Politècnica de València (UPV)InglésengMinisterio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 PT13%2F0001%2F0008 PLATAFORMA DE RECURSOS BIOMOLECULARES Y BIOINFORMATICOS, PRB2Ministerio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 AGL2011-24524 SEÑALIZACION POR ESPECIES REACTIVAS DE OXIGENO%2FNITROGENO Y ANTIOXIDANTES EN LA SIMBIOSIS FIJADORA DE NITROGENO RHIZOBIUM-LEGUMINOSAAgence Nationale de la Recherche, Francia https://doi.org/10.13039/501100001665 ANR-11-LABX-0002 Recherches Avancées sur l'Arbre et les Ecosytèmes ForestiersMinisterio de Economía y Competitividad http://dx.doi.org/10.13039/501100003329 AGL2014-53717-R FIJACION DE NITROGENO POR LA SIMBIOSIS RIZOBIO-LEGUMINOSA: HEMOGLOBINAS Y MODIFICACIONES OXIDATIVAS DE LAS PROTEINAS DURANTE EL DESARROLLO Y SENESCENCIA DE LOS NODULOSopen accesshttp://purl.org/coar/access_right/c_abf2Reserva de todos los derechoshttp://rightsstatements.org/vocab/InC/1.0/info:eu-repo/semantics/openAccessoai:riunet.upv.es:10251/678992026-06-13T07:49:27Z
score 15,300724

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